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Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles

The C-terminal domains of the Frizzleds (FZDs) contain a short conserved motif (KTXXXW). It has been demonstrated that FZDs interacted with the PDZ domain of the cytoplasmic proteins such as Dishevelled through this motif and mutations in this motif disrupted Wnt/β-catenin signaling. We carried out...

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Autores principales: Gayen, Shovanlal, Li, Qingxin, Kim, Young Mee, Kang, CongBao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6269726/
https://www.ncbi.nlm.nih.gov/pubmed/23881048
http://dx.doi.org/10.3390/molecules18078579
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author Gayen, Shovanlal
Li, Qingxin
Kim, Young Mee
Kang, CongBao
author_facet Gayen, Shovanlal
Li, Qingxin
Kim, Young Mee
Kang, CongBao
author_sort Gayen, Shovanlal
collection PubMed
description The C-terminal domains of the Frizzleds (FZDs) contain a short conserved motif (KTXXXW). It has been demonstrated that FZDs interacted with the PDZ domain of the cytoplasmic proteins such as Dishevelled through this motif and mutations in this motif disrupted Wnt/β-catenin signaling. We carried out structural studies for a peptide derived from the C-terminal domain of the FZD(1) in different solvents using circular dichroism and solution NMR spectroscopy. Our results showed that this domain was unstructured in an aqueous solution and formed a helical structure in detergent micelles. Fluorescence studies suggested that the tryptophan residue (W630) in the motif interacted with micelles. The solution structure of the peptide in sodium dodecyl sulfate micelles was determined and an amphipathic helix was identified. This helix may have similar function to the helix 8 of other G protein-coupled receptors.
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spelling pubmed-62697262018-12-17 Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles Gayen, Shovanlal Li, Qingxin Kim, Young Mee Kang, CongBao Molecules Article The C-terminal domains of the Frizzleds (FZDs) contain a short conserved motif (KTXXXW). It has been demonstrated that FZDs interacted with the PDZ domain of the cytoplasmic proteins such as Dishevelled through this motif and mutations in this motif disrupted Wnt/β-catenin signaling. We carried out structural studies for a peptide derived from the C-terminal domain of the FZD(1) in different solvents using circular dichroism and solution NMR spectroscopy. Our results showed that this domain was unstructured in an aqueous solution and formed a helical structure in detergent micelles. Fluorescence studies suggested that the tryptophan residue (W630) in the motif interacted with micelles. The solution structure of the peptide in sodium dodecyl sulfate micelles was determined and an amphipathic helix was identified. This helix may have similar function to the helix 8 of other G protein-coupled receptors. MDPI 2013-07-22 /pmc/articles/PMC6269726/ /pubmed/23881048 http://dx.doi.org/10.3390/molecules18078579 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Gayen, Shovanlal
Li, Qingxin
Kim, Young Mee
Kang, CongBao
Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title_full Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title_fullStr Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title_full_unstemmed Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title_short Structure of the C-terminal Region of the Frizzled Receptor 1 in Detergent Micelles
title_sort structure of the c-terminal region of the frizzled receptor 1 in detergent micelles
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6269726/
https://www.ncbi.nlm.nih.gov/pubmed/23881048
http://dx.doi.org/10.3390/molecules18078579
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